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Int J Biol Macromol. 2012 Apr 1;50(3):573-7. doi: 10.1016/j.ijbiomac.2012.01.030. Epub 2012 Jan 31.

The inhibitory effect of ethylenediamine on mushroom tyrosinase.

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Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.


The inhibitory effect of ethylenediamine on both activities of mushroom tyrosinase (MT) at 20 °C in a 10 mM phosphate buffer solution (pH 6.8), was studied. L-DOPA and L-tyrosine were used as substrates of catecholase and cresolase activities, respectively. The results showed that ethylenediamine competitively inhibits both activities of the enzyme with inhibition constants (K(i)) of 0.18±0.05 and 0.14±0.01 μM for catecholase and cresolase respectively, which are lower than the reported values for other MT inhibitors. For further insight a docking study between tyrosinase and ethylenediamine was performed. The docking simulation showed that ethylenediamine binds in the active site of the enzyme near the Cu atoms and makes 3 hydrogen bonds with two histidine residues of active site.

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